PDBsum entry 3j9e

Viral protein

PDB id: 3j9e

Contents

Protein chain

520 a.a.

PDB id:

3j9e

Name:

Viral protein

Title:

Atomic structure of a non-enveloped virus reveals ph sensors for a coordinated process of cell entry

Structure:

Vp5. Chain: d

Source:

Bluetongue virus 1. Organism_taxid: 35327

Authors:

X.Zhang,A.Patel,C.Celma,P.Roy,Z.H.Zhou

Key ref:

X.Zhang et al. (2016). Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry. Nat Struct Biol, 23, 74-80. PubMed id: 26641711 DOI: 10.1038/nsmb.3134

Date:

10-Jan-15 Release date: 09-Dec-15

Protein chain

K7QP12  (K7QP12_9REOV) -  Outer capsid protein VP5 from Bluetongue virus 1

Seq: 526 a.a.

Struc: 520 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsmb.3134

Nat Struct Biol 23:74-80 (2016)

PubMed id: 26641711

Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.

X.Zhang, A.Patel, C.C.Celma, X.Yu, P.Roy, Z.H.Zhou.

ABSTRACT

Viruses sense environmental cues such as pH to engage in membrane interactions for cell entry during infection, but how nonenveloped viruses sense pH is largely undefined. Here, we report both high- and low-pH structures of bluetongue virus (BTV), which enters cells via a two-stage endosomal process. The receptor-binding protein VP2 possesses a zinc finger that may function to maintain VP2 in a metastable state and a conserved His866, which senses early-endosomal pH. The membrane-penetration protein VP5 has three domains: dagger, unfurling and anchoring. Notably, the β-meander motif of the anchoring domain contains a histidine cluster that can sense late-endosomal pH and also possesses four putative membrane-interaction elements. Exposing BTV to low pH detaches VP2 and dramatically refolds the dagger and unfurling domains of VP5. Our biochemical and structure-guided-mutagenesis studies support these coordinated pH-sensing mechanisms.